3.4.21.104: mannan-binding lectin-associated serine protease-2
This is an abbreviated version!
For detailed information about mannan-binding lectin-associated serine protease-2, go to the full flat file.
Word Map on EC 3.4.21.104
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3.4.21.104
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masps
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spider
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silk
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ficolins
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ampullate
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dragline
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spidroins
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c1s
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clavipes
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nephila
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collectins
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m-ficolin
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widow
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hesperus
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latrodectus
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medicine
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molecular biology
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diagnostics
- 3.4.21.104
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masps
- spider
-
silk
- ficolins
-
ampullate
-
dragline
-
spidroins
- c1s
- clavipes
- nephila
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collectins
- m-ficolin
- widow
- hesperus
- latrodectus
- medicine
- molecular biology
- diagnostics
Reaction
Selective cleavage after Arg223 in complement component C2 (-Ser-Leu-Gly-Arg-/-Lys-Ile-Gln-Ile) and after Arg76 in complement component C4 (-Gly-Leu-Gln-Arg-/-Ala-Leu-Glu-Ile) =
Synonyms
CCP1-CCP2-SP, Mannan-binding lectin associated serine protease-2, mannan-binding lectin-associated serine protease, mannan-binding lectin-associated serine protease 2, mannan-binding lectin-associated serine protease-2, mannose-binding lectin-associated serine protease 2, mannose-binding lectin-associated serine protease-2, mannose-binding lectin-associated-serine protease-2, Map19, MASP, MASP-2, MASP-2A, MASP-2K, MASP2, MBL-associated serine protease, MBL-associated serine protease 2, MBL-associated serine protease-2, MBL-associated-serine protease-2, MBL-MASP, MBL/ficolin-associated serine protease, MBP-associated serine protease, MBP-associated serine protease 2, MBP-associated serine protease-2, S01.229
ECTree
3.4.21.104 mannan-binding lectin-associated serine protease-2Advanced search results
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results (Engineering
Engineering on EC 3.4.21.104 - mannan-binding lectin-associated serine protease-2
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C1s(MASP-2CCP1/2)
hybrid C1s/MASP-2 molecule, swapped complement control protein, 21-27fold higher kcat/Km-ratio for complement C4 than C1s(MASP-2SP)
C1s(MASP-2SP)
hybrid C1s/MASP-2 molecule, swapped serine protease, 21-27fold lower kcat/Km-ratio for complement C4 than C1s(MASP-2CCP1/2)
D105G
D120G
H155R
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the mutant cleaves complement component C4 slightly better than the wild type MASP-2
P111L
found in 4% of studied North Africans, not found in Sub-Saharans and Spaniards
P126L
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the mutant cleaves complement component C4 with an activity comparable to wild type MASP-2
R103C
found in 2% of studied North Africans, not found in Sub-Saharans and Spaniards
R439H
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the mutant is deficient in cleavage of complement component C4 despite its normal binding to mannan-binding lectin, the mutant is not able to autoactivate in the presence of mannan-binding lectin and mannan
R84Q
found in 13.33% of studied Sub-Saharans, 1% of studied North Africans, not found in Spaniards
R99Q
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the mutant cleaves complement component C4 with an activity comparable to wild type MASP-2
V377A
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the mutant cleaves complement component C4 with an activity comparable to wild type MASP-2
R424K
S613A
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site-directed mutagenesis, the mutant zymogen cannot autoactivate and is secreted in the zymogen form
additional information
D105G
inactive, MASP-2 deficiency, the index case suffers from recurrent severe infections and autoimmune reactions
D105G
incapable of forming a complex with mannan-binding lectin, found in 1.44% of studied Spaniards, 2% of studied North Africans, not found in Sub-Saharans
D105G
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it is investigated whether partial or total MASP-2 deficiencies resulting from D105G mutation are associated with rheumatic fever and chronic rheumatic heart disease: 148 patients are analyzed with a history of rheumatic fever, including 106 with chronic rheumatic heart and 42 without cardiac sequelae, and 129 control subjects. The D105G mutation is detected in four patients with chronic rheumatic heart and in five control subjects , all in the heterozygous state. None of the patients without cardiac sequelae has the mutation. No significant difference is found in the frequency of the mutant allele between the groups. D105G mutation in the MASP2 gene does not play a major role in the pathogenesis of rheumatic fever
D105G
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the mutation causes impaired binding to mannan-binding lectin and low circulating plasma levels of MASP-2
D120G
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among 362 samples tested for the D120G single nucleotide polymorphism of the MASP2 gene, no homozygote for that mutation is found. Heterozygosity for this allele significantly influences the protein concentration, but not the lectin pathway of complement activity (MBL-MASP-2 complex activity). No association of this single nucleotide polymorphism is apparent with prematurity, low birth weight or perinatal infections
D120G
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when D120G is mixed with mannan-binding lectin, no activation of complement component C4 is observed
R424K
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site-directed mutagenesis, mutation at the zymogen cleavage site, yielding an active form of MASP2 that is secreted as zymogen but is more stable than wild-type MASP2, since it only autoactivates in complex with MBL upon binding to a suitable surface
R424K
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site-directed mutagenesis, the mutant shows a reduced autoactivation rate, due to more slowly autoactivation reaction compared to the wild-type enzyme, with reduced zymogen activation during biosynthesis, secretion, and purification
additional information
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serum depleted of MASP-1, MASP-2 and MASP-3, shows synergetic effect of reconstitution with MASP-1 and MASP-2, overview
additional information
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transcription activity is decreased 5fold when the StatB binding site of the MASP-2 promoter is mutated in the wild-type reporter gene construct
additional information
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when the mutant enzyme 156_159dupCHNH (CHNHdup) is mixed with mannan-binding lectin, no activation of complement component C4 is observed
additional information
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construction of MASP-2-deficient mice, MASP-2-deficient mice show reduced activity for C3 deposition on the surface of mannan and zymosan, lectin complement pathway and phenotype, overview
additional information
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when recombinant sMAP and recombinant MASP-2 reconstitute the MBL-MASP-sMAP complex in deficient serum, the binding of these recombinant proteins to MBL is competitive, and the C4 cleavage activity of the MBL-MASP-sMAP complex is restored by the addition of rMASP-2, whereas the addition of rsMAP attenuates the activity
additional information
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construction of an enzymatically inactive enzyme, also not exhibiting autocatalytic activity, by substitution of the active size catalytic Ser residue with alanine, i.e. MASP-2A, construction of a zymogen with reduced autoproteolytic activity by substitution of the Arg residue at the autocatalytic cleavage site with lysine, i.e. MASP-2K
